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Conserved domains on  [gi|451327636|ref|NP_001263409|]
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lon protease homolog, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

endopeptidase La( domain architecture ID 11489643)

endopeptidase La is an ATP-dependent serine protease that degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long; it binds to DNA in a double-stranded, site-specific manner

CATH:  1.10.8.60
EC:  3.4.21.53
Gene Ontology:  GO:0005524|GO:0016887|GO:0004176|GO:0004252|GO:0043565
MEROPS:  S16
PubMed:  34563541|9115177

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 6-751 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


:

Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1124.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636    6 DKLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVHE 85
Cdd:TIGR00763  79 ATYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   86 DFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKRL 163
Cdd:TIGR00763 114 PFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKRL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  164 YKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVVD 243
Cdd:TIGR00763 192 KKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVIE 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  244 EELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKIL 323
Cdd:TIGR00763 271 KELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPIL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  324 CFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGY 403
Cdd:TIGR00763 351 CLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSF 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  404 QGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQAR 483
Cdd:TIGR00763 431 RGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKAL 510

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  484 ALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFTV 557
Cdd:TIGR00763 511 EDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFTY 590

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  558 ERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAND 637
Cdd:TIGR00763 591 ERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPN 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  638 YLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLP 717
Cdd:TIGR00763 662 FFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILP 741

                         730       740       750
                  ....*....|....*....|....*....|....
gi 451327636  718 AENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 751
Cdd:TIGR00763 742 EKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 6-751 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1124.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636    6 DKLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVHE 85
Cdd:TIGR00763  79 ATYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   86 DFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKRL 163
Cdd:TIGR00763 114 PFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKRL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  164 YKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVVD 243
Cdd:TIGR00763 192 KKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVIE 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  244 EELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKIL 323
Cdd:TIGR00763 271 KELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPIL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  324 CFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGY 403
Cdd:TIGR00763 351 CLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSF 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  404 QGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQAR 483
Cdd:TIGR00763 431 RGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKAL 510

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  484 ALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFTV 557
Cdd:TIGR00763 511 EDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFTY 590

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  558 ERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAND 637
Cdd:TIGR00763 591 ERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPN 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  638 YLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLP 717
Cdd:TIGR00763 662 FFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILP 741

                         730       740       750
                  ....*....|....*....|....*....|....
gi 451327636  718 AENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 751
Cdd:TIGR00763 742 EKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 75-754 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 981.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  75 LMVEVEnVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVL 154
Cdd:COG0466  113 LEAEVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 155 EETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVV 234
Cdd:COG0466  188 ETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 235 PKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQL 314
Cdd:COG0466  267 PEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKL 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 315 RGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILID 394
Cdd:COG0466  347 KKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLD 426

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 395 EVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIA 474
Cdd:COG0466  427 EIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIA 506

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 475 ERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPV 554
Cdd:COG0466  507 KRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPR 586

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 555 FTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAP 634
Cdd:COG0466  587 FRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATL-------MPG--KGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 657

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 635 ANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCI 714
Cdd:COG0466  658 DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTV 737

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|
gi 451327636 715 VLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDE 754
Cdd:COG0466  738 ILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 129-751 4.68e-178

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 529.51  E-value: 4.68e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 129 VDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 208
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 209 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQ 288
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 289 AVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRT 368
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 369 YVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 448
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 449 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSA 528
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 529 YKIVSGEA-ESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETslrrpqdkdAKGDKDGSLEVT 607
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIET---------ACVPGKGKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 608 GQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEV 687
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451327636 688 SLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 751
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 284-465 1.51e-130

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 384.99  E-value: 1.51e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 284 LARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIK 363
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 364 GHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 443
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                        170       180
                 ....*....|....*....|..
gi 451327636 444 NVTDTIPEPLRDRMEMINVSGY 465
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 541-752 1.34e-80

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 256.40  E-value: 1.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  541 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRrpqdkdakgDKDGSLEVTGQLGEVMKESARI 620
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM---------PGKGKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  621 AYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIK 700
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 451327636  701 EKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFP 752
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 319-456 2.82e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.23  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   319 QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRR-----------TYVGAMPGKIIQCLKKTKte 387
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivggkkasGSGELRLRLALALARKLK-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   388 NPLILIDEVDKIGRgyqgDPSSALLELLDPEQNANFLDHYLDVPVdlskvlfICTAN-VTDTIPEPLRDR 456
Cdd:smart00382  79 PDVLILDEITSLLD----AEQEALLLLLEELRLLLLLKSEKNLTV-------ILTTNdEKDLGPALLRRR 137
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 6-751 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1124.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636    6 DKLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVHE 85
Cdd:TIGR00763  79 ATYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKEE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   86 DFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKRL 163
Cdd:TIGR00763 114 PFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKRL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  164 YKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVVD 243
Cdd:TIGR00763 192 KKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVIE 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  244 EELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKIL 323
Cdd:TIGR00763 271 KELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPIL 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  324 CFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGY 403
Cdd:TIGR00763 351 CLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSF 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  404 QGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQAR 483
Cdd:TIGR00763 431 RGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKAL 510

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  484 ALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFTV 557
Cdd:TIGR00763 511 EDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFTY 590

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  558 ERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAND 637
Cdd:TIGR00763 591 ERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPN 661

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  638 YLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLP 717
Cdd:TIGR00763 662 FFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILP 741

                         730       740       750
                  ....*....|....*....|....*....|....
gi 451327636  718 AENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 751
Cdd:TIGR00763 742 EKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 75-754 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 981.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  75 LMVEVEnVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVL 154
Cdd:COG0466  113 LEAEVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 155 EETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVV 234
Cdd:COG0466  188 ETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 235 PKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQL 314
Cdd:COG0466  267 PEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKL 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 315 RGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILID 394
Cdd:COG0466  347 KKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLD 426

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 395 EVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIA 474
Cdd:COG0466  427 EIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIA 506

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 475 ERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPV 554
Cdd:COG0466  507 KRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPR 586

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 555 FTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAP 634
Cdd:COG0466  587 FRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATL-------MPG--KGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 657

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 635 ANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCI 714
Cdd:COG0466  658 DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTV 737

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|
gi 451327636 715 VLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDE 754
Cdd:COG0466  738 ILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 129-751 4.68e-178

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 529.51  E-value: 4.68e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 129 VDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 208
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 209 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQ 288
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 289 AVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRT 368
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 369 YVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 448
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 449 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSA 528
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 529 YKIVSGEA-ESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETslrrpqdkdAKGDKDGSLEVT 607
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIET---------ACVPGKGKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 608 GQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEV 687
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451327636 688 SLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 751
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 284-465 1.51e-130

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 384.99  E-value: 1.51e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 284 LARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIK 363
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 364 GHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 443
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                        170       180
                 ....*....|....*....|..
gi 451327636 444 NVTDTIPEPLRDRMEMINVSGY 465
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 541-752 1.34e-80

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 256.40  E-value: 1.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  541 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRrpqdkdakgDKDGSLEVTGQLGEVMKESARI 620
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM---------PGKGKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  621 AYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIK 700
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 451327636  701 EKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFP 752
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 323-465 6.27e-32

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 120.39  E-value: 6.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  323 LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 401
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451327636  402 -------GYQGDPSSALLELLDPEQNANfldhyldvpvdlSKVLFICTANVTDTIPEPLRDRMEMINVSGY 465
Cdd:pfam00004  72 srgsggdSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 301-462 2.05e-19

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 85.80  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 301 VKKRILEFIAV------SQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAeikghrRTYVGAMP 374
Cdd:cd19481    1 LKASLREAVEAprrgsrLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 375 GKIIQCLKKTKteNPLILIDEVDKIG--RGYQGDPS------SALLELLDPEQNanfldhyldvpvdLSKVLFICTAN-V 445
Cdd:cd19481   75 RKIFERARRLA--PCILFIDEIDAIGrkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNrP 139

                        170
                 ....*....|....*....
gi 451327636 446 TDTIPEPLR--DRMEMINV 462
Cdd:cd19481  140 DLLDPALLRpgRFDEVIEF 158
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
611-725 5.31e-18

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 83.49  E-value: 5.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 611 GEVMKESARIAytFARAFLMQHAPANDYLVTSHIhlhvpEGATPK-DGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSL 689
Cdd:COG1750   69 GPDTQASARIA--ALVASLLAGVDLSSYDVYISI-----ESDSPIvGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINP 141

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 451327636 690 TGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFY 725
Cdd:COG1750  142 DGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTG 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 296-460 1.02e-15

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 74.88  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 296 YGMEDVKKRILEFIAvsqlrgSTQGKILCFYGPPGVGKTSIARSIARALNREYFRF---SVGGMTDVAEIKGHRRTYVGA 372
Cdd:cd00009    1 VGQEEAIEALREALE------LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 373 MPGKIIQclkktKTENPLILIDEVDKIGRGYQgdpssallelldpEQNANFLDHYLDVPVDLSKVLFICTANVTD--TIP 450
Cdd:cd00009   75 LLFELAE-----KAKPGVLFIDEIDSLSRGAQ-------------NALLRVLETLNDLRIDRENVRVIGATNRPLlgDLD 136

                        170
                 ....*....|
gi 451327636 451 EPLRDRMEMI 460
Cdd:cd00009  137 RALYDRLDIR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 297-478 3.27e-15

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 78.41  E-value: 3.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFIA-------VSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrTY 369
Cdd:COG0464  161 GLEEVKEELRELVAlplkrpeLREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS---------KY 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 370 VGAMPGKIIQCLKKTKTENPLIL-IDEVDKI--GRGYQGDPS-----SALLELLDpeqnanfldhylDVPvdlSKVLFIC 441
Cdd:COG0464  232 VGETEKNLREVFDKARGLAPCVLfIDEADALagKRGEVGDGVgrrvvNTLLTEME------------ELR---SDVVVIA 296

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 451327636 442 TANVTDTIPEPLRDRM-EMINVSGYVAQEKLAIAERYL 478
Cdd:COG0464  297 ATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHL 334
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
293-478 4.29e-12

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 66.83  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 293 EDHYGMEDVKKRILEFIA----VSQLRG---STQGKILcFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikgh 365
Cdd:COG1223    2 DDVVGQEEAKKKLKLIIKelrrRENLRKfglWPPRKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 366 rrTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIG--RGYQ---GDPS---SALLELLDPEQnanfldhyldvpvdlSKV 437
Cdd:COG1223   74 --SYLGETARNLRKLFDFARRAPCVIFFDEFDAIAkdRGDQndvGEVKrvvNALLQELDGLP---------------SGS 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 451327636 438 LFICTANVTDTIPEPLRDRMEM-INVSGYVAQEKLAIAERYL 478
Cdd:COG1223  137 VVIAATNHPELLDSALWRRFDEvIEFPLPDKEERKEILELNL 178
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 75-172 1.31e-09

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 58.50  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   75 LMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYrESVLQMMqagqrVVDNPIYLSDMGAALTGAESHELQDVL 154
Cdd:pfam02190 104 LRAEVEDLPEDSDELSEALKALVKELIEKLRRLLKLLLPL-ELLLKIK-----DIENPGRLADLVAAILPLSPEEKQELL 177

                          90
                  ....*....|....*...
gi 451327636  155 EETNIPKRLYKALSLLKK 172
Cdd:pfam02190 178 ETLDVKERLEKVLELLNR 195
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 323-457 2.39e-09

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 56.15  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  323 LCFYGPPGVGKTSIARSIARAL-NREYFRFSVGGMTDVAEIKGHRRTYVGAmPGKIIQCLKKTKTENPLILIDEVDKIGR 401
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGG-ASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451327636  402 GYQGdpssALLELLDPEQ----NANFLdhyldVPVDLSKVLFICTANVTDT----IPEPLRDRM 457
Cdd:pfam07728  81 DVLN----SLLSLLDERRlllpDGGEL-----VKAAPDGFRLIATMNPLDRglneLSPALRSRF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 325-396 2.46e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.46e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451327636 325 FYGPPGVGKTSIARSIARALNREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKT--ENPLILIDEV 396
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALS-AVTSGVKDLR------------EVIEEARQRRSagRRTILFIDEI 101
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 319-456 2.82e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 56.23  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   319 QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRR-----------TYVGAMPGKIIQCLKKTKte 387
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivggkkasGSGELRLRLALALARKLK-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636   388 NPLILIDEVDKIGRgyqgDPSSALLELLDPEQNANFLDHYLDVPVdlskvlfICTAN-VTDTIPEPLRDR 456
Cdd:smart00382  79 PDVLILDEITSLLD----AEQEALLLLLEELRLLLLLKSEKNLTV-------ILTTNdEKDLGPALLRRR 137
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 297-458 2.64e-08

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 53.90  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFI--------AVSQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrT 368
Cdd:cd19509    3 GLDDAKEALKEAVilpslrpdLFPGLRGPPRGILL--YGPPGTGKTLLARAVASESGSTFFSISASSLVS---------K 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 369 YVGAmPGKIIQCLKKTKTEN--PLILIDEVDKIGRGYQGDPSSA-------LLELLDPEQNAnfldhyldvpvDLSKVLF 439
Cdd:cd19509   72 WVGE-SEKIVRALFALARELqpSIIFIDEIDSLLSERGSGEHEAsrrvkteFLVQMDGVLNK-----------PEDRVLV 139

                        170
                 ....*....|....*....
gi 451327636 440 ICTANVTDTIPEPLRDRME 458
Cdd:cd19509  140 LGATNRPWELDEAFLRRFE 158
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 325-445 5.06e-08

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 53.35  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  325 FYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEikghrRTYV----GAMPGKI------IQCLKKTKTENPLILID 394
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFGDERALIRIDMSEYME-----EHSVsrliGAPPGYVgyeeggQLTEAVRRKPYSIVLID 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 451327636  395 EVDKIGRGYQgdpsSALLELLDpeqNANFLDHYlDVPVDLSKVLFICTANV 445
Cdd:pfam07724  83 EIEKAHPGVQ----NDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNF 125
44 PHA02544
clamp loader, small subunit; Provisional
 299-507 6.12e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 55.00  E-value: 6.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 299 EDVKKRILEFIavsqlrgsTQGKI--LCFYGP-PGVGKTSIARSIARALNREYFrFSVGGMTDVAEIKGHRRTYVGAM-- 373
Cdd:PHA02544  27 AADKETFKSIV--------KKGRIpnMLLHSPsPGTGKTTVAKALCNEVGAEVL-FVNGSDCRIDFVRNRLTRFASTVsl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 374 --PGKIiqclkktktenplILIDEVDKIGRgyqgdpSSALLELldpeqnANFLDHYldvpvdlSK-VLFICTANVTDTIP 450
Cdd:PHA02544  98 tgGGKV-------------IIIDEFDRLGL------ADAQRHL------RSFMEAY-------SKnCSFIITANNKNGII 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 451327636 451 EPLRDRMEMINVSGYVAQEKLAIAERYLVpqaRALCGLDESKAKLSSDVLTLLIKQY 507
Cdd:PHA02544 146 EPLRSRCRVIDFGVPTKEEQIEMMKQMIV---RCKGILEAEGVEVDMKVLAALVKKN 199
PRK04195 PRK04195
replication factor C large subunit; Provisional
 297-506 6.24e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 55.70  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFIAvSQLRGSTQgKILCFYGPPGVGKTSIARSIARALNREYF-------------RFSVGGMTDVAEIK 363
Cdd:PRK04195  18 GNEKAKEQLREWIE-SWLKGKPK-KALLLYGPPGVGKTSLAHALANDYGWEVIelnasdqrtadviERVAGEAATSGSLF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 364 GHRRTyvgampgkiiqclkktktenpLILIDEVDKI-GRGYQGDpSSALLELLDpeqNANfldhyldVPVdlskvlfICT 442
Cdd:PRK04195  96 GARRK---------------------LILLDEVDGIhGNEDRGG-ARAILELIK---KAK-------QPI-------ILT 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451327636 443 AN-VTDTIPEPLRDRMEMINVSgyvaqeklAIAERYLVPQARALCGLDesKAKLSSDVLTLLIKQ 506
Cdd:PRK04195 137 ANdPYDPSLRELRNACLMIEFK--------RLSTRSIVPVLKRICRKE--GIECDDEALKEIAER 191
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 325-396 1.93e-07

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 54.29  E-value: 1.93e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451327636 325 FYGPPGVGKTSIARSIARALNREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKTEN--PLILIDEV 396
Cdd:COG2256   54 LWGPPGTGKTTLARLIANATDAEFVALS-AVTSGVKDIR------------EVIEEARERRAYGrrTILFVDEI 114
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 201-401 2.17e-07

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.47  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 201 QEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVvdeELSKLGLLDNHSSEFNVTRNYLDWLTSipwgkysne 280
Cdd:COG1222    1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALEL---LEEAPALLLNDANLTQKRLGTPRGTAV--------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 281 nldLARAQAVLEEDHYGMEDVKKRILEFIAVSQLR-------GSTQGKILCFYGPPGVGKTSIARSIARALNREYFRfsV 353
Cdd:COG1222   69 ---PAESPDVTFDDIGGLDEQIEEIREAVELPLKNpelfrkyGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIR--V 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 451327636 354 GGmtdvAEIkghRRTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 401
Cdd:COG1222  144 RG----SEL---VSKYIGEGARNVREVFELAREKAPsIIFIDEIDAIAA 185
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 656-702 8.74e-07

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 52.64  E-value: 8.74e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 451327636 656 DGPSAGCTIVTALLSlAMGR-PVRQNLAMTGEVSLTGKILPVGGIKEK 702
Cdd:COG1067  592 DGDSASSAELYALLS-ALSGvPIRQDIAVTGSVNQHGEVQPIGGVNEK 638
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 293-477 9.76e-07

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 51.15  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  293 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALNREyFRFSVGGMTDvaeikghrrtyvga 372
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALE-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  373 MPGKIIQCLKKTKtENPLILIDEVDKIGRgyqgdpssALLELLDPEQNANFLDHYLD-------VPVDLSKVLFICTANV 445
Cdd:TIGR00635  68 KPGDLAAILTNLE-EGDVLFIDEIHRLSP--------AVEELLYPAMEDFRLDIVIGkgpsarsVRLDLPPFTLVGATTR 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 451327636  446 TDTIPEPLRDRMEMI-NVSGYVAQEKLAIAERY 477
Cdd:TIGR00635 139 AGMLTSPLRDRFGIIlRLEFYTVEELAEIVSRS 171
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
654-720 1.80e-06

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 47.44  E-value: 1.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 451327636  654 PKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAEN 720
Cdd:pfam13541  55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 297-454 2.29e-06

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 48.44  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFIAvSQLRGSTQGKIL--------CFYGPPGVGKTSIARSIARALNREYFrfsvggmtdvaEIKGHrrT 368
Cdd:cd19503    4 GLDEQIASLKELIE-LPLKYPELFRALglkpprgvLLHGPPGTGKTLLARAVANEAGANFL-----------SISGP--S 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 369 YVGAMPGKIIQCLKK-----TKTENPLILIDEVDKIG--RGY-QGDPS----SALLELLDPEQNANfldhyldvpvdlsK 436
Cdd:cd19503   70 IVSKYLGESEKNLREifeeaRSHAPSIIFIDEIDALApkREEdQREVErrvvAQLLTLMDGMSSRG-------------K 136

                        170
                 ....*....|....*...
gi 451327636 437 VLFICTANVTDTIPEPLR 454
Cdd:cd19503  137 VVVIAATNRPDAIDPALR 154
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
657-737 3.94e-06

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 49.81  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 657 GPSAGctivtaL-LSLAM-----------GRPVrqnlAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENkkdf 724
Cdd:COG3480  240 GPSAG------LmFALGIydqltpgdltgGKKI----AGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---- 305

                         90
                 ....*....|....
gi 451327636 725 YDLA-AFITEGLEV 737
Cdd:COG3480  306 CAEAvGTIPTGLKV 319
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
293-345 4.74e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.36  E-value: 4.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451327636 293 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 345
Cdd:PRK00080  25 DEFIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLANIIANEMG 76
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 293-345 5.18e-06

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 47.11  E-value: 5.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 451327636  293 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 345
Cdd:pfam05496   7 DEYIGQEKVKENLKIFIEAAKQRGEALDHVL-LYGPPGLGKTTLANIIANEMG 58
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 297-401 5.45e-06

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 47.23  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFiaVSQLRGSTQ-----GKI---LCFYGPPGVGKTSIARSIARALNREYfrFSVGGmTDVAEIkghrrt 368
Cdd:cd19501    8 GCEEAKEELKEV--VEFLKNPEKftklgAKIpkgVLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM------ 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 451327636 369 YVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 401
Cdd:cd19501   77 FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVGR 110
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 130-169 6.47e-06

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 45.12  E-value: 6.47e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 451327636   130 DNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSL 169
Cdd:smart00464  53 ETPEPLSDTIAALMPLELHEKQELLELEGTNKRLEKVIKL 92
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 327-416 8.59e-06

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.24  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 327 GPPGVGKTSIARSIARALNREYFR--FSVGGM------TDVAEIKGHRRTYVgamPGKIIQclkktktenPLILIDEVDK 398
Cdd:COG0714   38 GVPGVGKTTLAKALARALGLPFIRiqFTPDLLpsdilgTYIYDQQTGEFEFR---PGPLFA---------NVLLADEINR 105

                         90       100
                 ....*....|....*....|
gi 451327636 399 igrgyqGDP--SSALLELLD 416
Cdd:COG0714  106 ------APPktQSALLEAME 119
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 327-454 2.08e-05

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 45.83  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 327 GPPGVGKTSIARSIARALNREYFRFSVGGMTDVAeikghrrtYVGAMPGKIIQCLKKTktenpLILIDEVDKI---GRGY 403
Cdd:cd19498   53 GPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVG--------YVGRDVESIIRDLVEG-----IVFIDEIDKIakrGGSS 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 451327636 404 QGDPSSALLE--LLDPEQNANFLDHYldVPVDLSKVLFICT-----ANVTDTIPE-----PLR 454
Cdd:cd19498  120 GPDVSREGVQrdLLPIVEGSTVSTKY--GPVKTDHILFIAAgafhvAKPSDLIPElqgrfPIR 180
ftsH CHL00176
cell division protein; Validated
 289-401 2.89e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 47.35  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 289 AVLEEDHYGMEDVKKRILEFiaVSQLR--------GSTQGKILCFYGPPGVGKTSIARSIARALNREYfrFSVGGMTDVA 360
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEV--VSFLKkperftavGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPF--FSISGSEFVE 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 451327636 361 EIKGhrrtyVGAmpGKIIQCLKKTKTENPLIL-IDEVDKIGR 401
Cdd:CHL00176 255 MFVG-----VGA--ARVRDLFKKAKENSPCIVfIDEIDAVGR 289
rfc PRK00440
replication factor C small subunit; Reviewed
 276-350 4.48e-05

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 46.40  E-value: 4.48e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 451327636 276 KYSNENLDlaraqavleeDHYGMEDVKKRILEFIAvsqlrgstQGKI--LCFYGPPGVGKTSIARSIARALNREYFR 350
Cdd:PRK00440  10 KYRPRTLD----------EIVGQEEIVERLKSYVK--------EKNMphLLFAGPPGTGKTTAALALARELYGEDWR 68
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 293-399 7.09e-05

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 44.21  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 293 EDHYGMEDVKKRILEFIAV--------SQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikg 364
Cdd:cd19525   22 ADIAGLEFAKKTIKEIVVWpmlrpdifTGLRGPPKGILL--FGPPGTGKTLIGKCIASQSGATFFSISASSLTS------ 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 451327636 365 hrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI 399
Cdd:cd19525   94 ---KWVGEGEKMVRALFSVARCKQPaVIFIDEIDSL 126
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 293-345 7.28e-05

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 45.46  E-value: 7.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451327636 293 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 345
Cdd:COG2255   28 DEYIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLAHIIANEMG 79
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 326-454 9.33e-05

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 43.64  E-value: 9.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 326 YGPPGVGKTSIARSIARALNREYfrFSVGGMTDVAEikghrrtYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI--GRG 402
Cdd:cd19529   33 YGPPGTGKTLLAKAVATESNANF--ISVKGPELLSK-------WVGESEKAIREIFRKARQVAPcVIFFDEIDSIapRRG 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 451327636 403 YQGDPSSAllelldpEQNANFLDHYLDVPVDLSKVLFICTANVTDTI-PEPLR 454
Cdd:cd19529  104 TTGDSGVT-------ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIdPALLR 149
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
325-345 1.35e-04

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 44.80  E-value: 1.35e-04
                         10        20
                 ....*....|....*....|.
gi 451327636 325 FYGPPGVGKTSIARSIARALN 345
Cdd:COG2812   37 FTGPRGVGKTTLARILAKALN 57
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 323-460 1.41e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 43.32  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 323 LCFYGPPGVGKTSIARSIARAL---NREYFRFSVGG---MTDVAEIKGHRRTYVGA-MPGKIIQCLKKtkteNP--LILI 393
Cdd:cd19499   44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEymeKHSVSRLIGAPPGYVGYtEGGQLTEAVRR----KPysVVLL 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 451327636 394 DEVDKIGRGYQGdpssALLELLDpeqNANFLDHYLDVpVDLSKVLFICTANVtdtIPEPLRDRMEMI 460
Cdd:cd19499  120 DEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSNH---FRPEFLNRIDEI 175
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 297-397 1.52e-04

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 43.18  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFI----------AVSQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaEIKGHR 366
Cdd:cd19520    4 GLDEVITELKELVilplqrpelfDNSRLLQPPKGVLL--YGPPGCGKTMLAKATAKEAGARFINLQVSSLTD--KWYGES 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 451327636 367 RTYVGAMPGKIIqclkktKTENPLILIDEVD 397
Cdd:cd19520   80 QKLVAAVFSLAS------KLQPSIIFIDEID 104
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 299-456 1.97e-04

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 43.20  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 299 EDVKKRILEFIAVSqLRGSTQG---------KILCFYGPPGVGKTSIARSIARALN-REYFRFSVGGMTdvaEIKGHR-- 366
Cdd:cd19508   23 SNLKSRLLDYVTTT-LLFSDKNvntnlitwnRLVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQLI---EINSHSlf 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 367 -------RTYVGAMPGKiIQCLKKTKTENPLILIDEVDKIgrGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLF 439
Cdd:cd19508   99 skwfsesGKLVTKMFQK-IQELIDDKDALVFVLIDEVESL--AAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVI 175

                        170
                 ....*....|....*..
gi 451327636 440 ICTANVTDTIPEPLRDR 456
Cdd:cd19508  176 LLTSNLLEKIDVAFVDR 192
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
294-401 2.51e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 44.64  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 294 DHYGMEDVKKRILEFIAVSQLRGSTQ---GKI---LCFYGPPGVGKTSIARSIARALNREYFRFSvggMTDVAEIkghrr 367
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQklgGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM----- 224

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 451327636 368 tYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 401
Cdd:PRK10733 225 -FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 301-406 2.55e-04

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 42.12  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 301 VKKRILEFIAVSQLR------GSTQGKILCFYGPPGVGKTSIARSIARALNREYfrFSVGGMTDVaeikghrRTYVGAMP 374
Cdd:cd19527    1 VKKEILDTIQLPLEHpelfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNF--LSVKGPELI-------NMYIGESE 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 451327636 375 GKIIQCLKKTKTENP-LILIDEVDKIG--RGYQGD 406
Cdd:cd19527   72 ANVREVFQKARDAKPcVIFFDELDSLApsRGNSGD 106
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 123-448 2.72e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.38  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 123 QAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQE 202
Cdd:COG1401   24 DAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 203 QLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIP-WGKYSNEN 281
Cdd:COG1401  104 LYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSAdALAAELSA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 282 LDLARAQAVLEEDHYGMEDVKKRILEFIA--VSQLRGSTQgKILcfYGPPGVGKTSIARSIARAL---NREYFRF----- 351
Cdd:COG1401  184 AEELYSEDLESEDDYLKDLLREKFEETLEafLAALKTKKN-VIL--AGPPGTGKTYLARRLAEALggeDNGRIEFvqfhp 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 352 ------SVGGMTDVAEIKGHRRTyvgamPGKIIQCLKKTKtENP----LILIDEvdkIGRG----YQGDpssaLLELLDP 417
Cdd:COG1401  261 swsyedFLLGYRPSLDEGKYEPT-----PGIFLRFCLKAE-KNPdkpyVLIIDE---INRAnvekYFGE----LLSLLES 327

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 451327636 418 EQNANFLD---HYLDVPVDLS---KVLFICTANVTDT 448
Cdd:COG1401  328 DKRGEELSielPYSGEGEEFSippNLYIIGTMNTDDR 364
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
 292-354 3.58e-04

PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.


Pssm-ID: 214810  Cd Length: 361  Bit Score: 43.43  E-value: 3.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 451327636   292 EEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALnREYFRFSVG 354
Cdd:smart00763  50 DHDFFGMEEAIERFVNYFKSAAQGLEERKQILYLLGPVGGGKSSLVECLKRGL-EEYSKTDEG 111
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 297-400 6.46e-04

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 41.24  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 297 GMEDVKKRILEFIA-------VSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFS----VGGMTdvaeikgh 365
Cdd:cd19518    4 GMDSTLKELCELLIhpilppeYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVS-------- 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 451327636 366 rrtyvGAMPGKIIQCLKKTKTENPLIL-IDEVDKIG 400
Cdd:cd19518   76 -----GESEEKIRELFDQAISNAPCIVfIDEIDAIT 106
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 326-399 8.36e-04

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 40.88  E-value: 8.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451327636 326 YGPPGVGKTSIARSIARALNReyFRFSVGGmtdvAEIKGhrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI 399
Cdd:cd19519   40 YGPPGTGKTLIARAVANETGA--FFFLING----PEIMS---KLAGESESNLRKAFEEAEKNAPaIIFIDEIDAI 105
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 323-348 2.23e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....*.
gi 451327636  323 LCFYGPPGVGKTSIARSIARALNREY 348
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 284-344 2.28e-03

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 41.37  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  284 LARAQAVLEEdHYGMEDVKKRI------LEFIAVSQLRG---STQGKILCFYGPPGVGKTSIARSIARAL 344
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVaalkssTAMALARAERGlpvAQTSNHMLFAGPPGTGKTTIARVVAKIY 336
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 325-416 2.34e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 39.19  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 325 FYGPPGVGKTSIARSIAralnreyfrfSVGGMTDVAeIKGHR--RTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIG- 400
Cdd:cd19511   32 LYGPPGCGKTLLAKALA----------SEAGLNFIS-VKGPElfSKYVGESERAVREIFQKARQAAPcIIFFDEIDSLAp 100

                         90       100
                 ....*....|....*....|...
gi 451327636 401 -RGYQGDPS------SALLELLD 416
Cdd:cd19511  101 rRGQSDSSGvtdrvvSQLLTELD 123
PRK13341 PRK13341
AAA family ATPase;
323-342 2.36e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.19  E-value: 2.36e-03
                         10        20
                 ....*....|....*....|
gi 451327636 323 LCFYGPPGVGKTSIARSIAR 342
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN 74
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 293-458 2.62e-03

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 39.46  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 293 EDHYGMEDVKKRILEF----IAVSQL----RGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikg 364
Cdd:cd19521    7 EDVAGLEGAKEALKEAvilpVKFPHLftgnRKPWSGILL--YGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 365 hrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGrGYQGDPSSALLELLDPEqnanFLDHYLDVPVDLSKVLFICTA 443
Cdd:cd19521   79 ---KWMGESEKLVKQLFAMARENKPsIIFIDEVDSLC-GTRGEGESEASRRIKTE----LLVQMNGVGNDSQGVLVLGAT 150

                        170
                 ....*....|....*
gi 451327636 444 NVTDTIPEPLRDRME 458
Cdd:cd19521  151 NIPWQLDSAIRRRFE 165
PRK15455 PRK15455
PrkA family serine protein kinase; Provisional
 293-337 2.65e-03

PrkA family serine protein kinase; Provisional


Pssm-ID: 185352 [Multi-domain]  Cd Length: 644  Bit Score: 41.12  E-value: 2.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 451327636 293 EDHYGMEDVKKRIlefiaVSQLRGSTQG-----KILCFYGPPGVGKTSIA 337
Cdd:PRK15455  76 EEFYGMEEAIEQI-----VSYFRHAAQGleekkQILYLLGPVGGGKSSLA 120
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 326-415 2.66e-03

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 39.24  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 326 YGPPGVGKTSIARSIARALNREYFRfsVGGMTDVaeikghrRTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGRGYQ 404
Cdd:cd19502   43 YGPPGTGKTLLAKAVANHTDATFIR--VVGSELV-------QKYIGEGARLVRELFEMAREKAPsIIFIDEIDAIGAKRF 113

                         90
                 ....*....|....*...
gi 451327636 405 GDPSSA-------LLELL 415
Cdd:cd19502  114 DSGTGGdrevqrtMLELL 131
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 319-354 2.67e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.41  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 451327636  319 QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVG 354
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 294-399 2.90e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 39.06  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 294 DHYGMEDVKKRILEFIAVSQLRGS------TQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrr 367
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPElftglrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS--------- 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 451327636 368 TYVGAMPgKIIQCLKKTKTE-NP-LILIDEVDKI 399
Cdd:cd19524   72 KYVGEGE-KLVRALFAVARElQPsIIFIDEVDSL 104
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
298-396 3.24e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 40.70  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 298 MEDVKKRILEFIavsqLRGSTQGKILCFYGPPGVGKTSIARSIARAL-NREYFRFsvggmtDVAEIkghrRTYVGAMPGK 376
Cdd:COG1373    2 MIMIKRKILDKL----LKLLDNRKAVVITGPRQVGKTTLLKQLAKELeNILYINL------DDPRL----RALAEEDPDD 67

                         90       100
                 ....*....|....*....|
gi 451327636 377 IIQCLKKTKTENPLILIDEV 396
Cdd:COG1373   68 LLEALKELYPGKTYLFLDEI 87
AAA_22 pfam13401
AAA domain;
315-415 3.50e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636  315 RGSTQGkILCFYGPPGVGKTSIARSIARAL---NREYFRFSVGGMTDVAEI----------KGHRRTYVGAMPGKIIQCL 381
Cdd:pfam13401   1 IRFGAG-ILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLlrallralglPLSGRLSKEELLAALQQLL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 451327636  382 KKTKTEnPLILIDEVDKIgrgyqgdpSSALLELL 415
Cdd:pfam13401  80 LALAVA-VVLIIDEAQHL--------SLEALEEL 104
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 304-453 3.66e-03

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 39.01  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 304 RILEFIAVSQLrGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGgmtdvAEIkghRRTYVGAMPGKIIQCLK- 382
Cdd:cd19504   20 RVFPPEIVEQL-GCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNG-----PEI---LNKYVGESEANIRKLFAd 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 383 -----KTKTENP---LILIDEVDKI--GRGYQGDPSSAllelldPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEP 452
Cdd:cd19504   91 aeeeqRRLGANSglhIIIFDEIDAIckQRGSMAGSTGV------HDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEA 164


                 .
gi 451327636 453 L 453
Cdd:cd19504  165 L 165
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
201-337 4.77e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.85  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 201 QEQLKIIKKELgleKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFnvtrnyldwltsipwgkysne 280
Cdd:COG1419   73 EEELEELRREL---AELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELAREL--------------------- 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 451327636 281 nldLARAQAVLEEDhYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKT-SIA 337
Cdd:COG1419  129 ---LEKLPEDLSAE-EAWRALLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTtTIA 182
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
325-463 5.60e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 39.57  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451327636 325 FYGPPGVGKTSIARSIARALNREY------------FRFSVGGMTDVAEIkghRRTYVGAMPGK-----IIQCLKKTKTE 387
Cdd:COG0470   23 LHGPPGIGKTTLALALARDLLCENpeggkacgqchsRLMAAGNHPDLLEL---NPEEKSDQIGIdqireLGEFLSLTPLE 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451327636 388 NP--LILIDEVDKIGRGYQgdpsSALLELL-DPEQNAnfldhyldvpvdlskvLFICTANVTDTIPEPLRDRMEMINVS 463
Cdd:COG0470  100 GGrkVVIIDEADAMNEAAA----NALLKTLeEPPKNT----------------PFILIANDPSRLLPTIRSRCQVIRFR 158
PRK06647 PRK06647
DNA polymerase III subunits gamma and tau; Validated
 307-345 7.16e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235845 [Multi-domain]  Cd Length: 563  Bit Score: 39.75  E-value: 7.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 451327636 307 EFIaVSQLRGSTQ-GKI---LCFYGPPGVGKTSIARSIARALN 345
Cdd:PRK06647  22 DFV-VETLKHSIEsNKIanaYIFSGPRGVGKTSSARAFARCLN 63
PRK06835 PRK06835
DNA replication protein DnaC; Validated
 298-344 7.22e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 39.11  E-value: 7.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 451327636 298 MEDVKKRILEFIAVSqlrgSTQGKILCFYGPPGVGKTSIARSIARAL 344
Cdd:PRK06835 165 MEKILEKCKNFIENF----DKNNENLLFYGNTGTGKTFLSNCIAKEL 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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